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作 者:沈如凌[1] 孙瑞林[2] 王庆诚 欧伶[1] 费俭
机构地区:[1]华东理工大学生物反应器工程国家重点实验室,上海200237 [2]中国科学院上海生命科学研究院,上海200031 [3]上海南方模式生物科技发展有限公司,上海201203
出 处:《细胞生物学杂志》2007年第6期901-904,共4页Chinese Journal of Cell Biology
基 金:上海市科学技术委员会重点项目资助(No.05DZ19322)~~
摘 要:Onconase(Onc)是一种从林蛙(Rana pipiens)卵细胞内提取的核酸酶,实验证实其在体外和体内对多种肿瘤细胞都具有显著的杀伤效果。在大肠杆菌中表达纯化的重组Onc和天然提取蛋白质具有相似的活性,通过测定该蛋白质对黑色素瘤B16细胞的IC50和建立荷瘤小鼠模型探讨了Onc体内外的抗肿瘤效果。实验结果表明:B16细胞在体外对Onc敏感性较K562细胞低,其IC50为6.37μmol/L;但体内每次每只小鼠给予5mg/kg Onc也可显著地抑制B16细胞的生长,延长小鼠的生存时间。实验提供了一种简化高效获得具有天然活性Onc的方法,同时通过Onc对低敏感性肿瘤黑色素瘤细胞的杀伤研究,丰富了对Onc抗肿瘤作用的认识,为治疗黑色素瘤提供了线索。Onconase, a ribonuclease firstly extracted from oocytes of frog (Rana pipiens), displays significant anti-tumor effects against many kinds of tumor cell lines in vivo and in vitro. We have expressed and purified the recombinant Onc in E.coli. The recombinant protein has similar activity as its natural form previously reported. The IC50 of the recombinant protein on B 16 cell was tested and its anti-tumor activity was studied on the B 16 melanoma animal model. The results showed that Onc has a pronounced effect on B 16 cell (IC50 = 6.37μmol/L), and greatly inhibits the growth of tumor cells and retard the mice's death. The experiment offers an efficient simple method to produce the recombinant Onc protein with similar activity as the natural one, and enriches the knowledge of Onc for its anti-tumor role and provides some clues for melanoma therapy.
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